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Conserved domains on  [gi|488881347|ref|WP_002793572|]
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c-type cytochrome [Campylobacter coli]

Protein Classification

Thioredoxin_like and Cytochrome_CBB3 domain-containing protein( domain architecture ID 10222164)

Thioredoxin_like and Cytochrome_CBB3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
57-82 5.66e-06

Cytochrome C oxidase, cbb3-type, subunit III;


:

Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 40.85  E-value: 5.66e-06
                          10        20
                  ....*....|....*....|....*.
gi 488881347   57 ANQRKGQQVYSKWCIACHGEGMPGTN 82
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAGPS 26
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-104 7.54e-03

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PRK03147:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 173  Bit Score: 34.21  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488881347   1 MKKIALFF---VLFVCLLNL------NAKDKEwlpkgESISVYEYIPNnprspAAFSSVDSKKLNANQRKGQQVY----S 67
Cdd:PRK03147   1 MKKNRLLFrtiILLILLAAVgytiysNFFADK-----EKVQVGKEAPN-----FVLTDLEGKKIELKDLKGKGVFlnfwG 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488881347  68 KWCIACHGEgMPGTNALSALYKDQG--IPALLEDRTDLS 104
Cdd:PRK03147  71 TWCKPCEKE-MPYMNELYPKYKEKGveIIAVNVDETELA 108
 
Name Accession Description Interval E-value
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
57-82 5.66e-06

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 40.85  E-value: 5.66e-06
                          10        20
                  ....*....|....*....|....*.
gi 488881347   57 ANQRKGQQVYSKWCIACHGEGMPGTN 82
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAGPS 26
CytC5 COG3245
Cytochrome c5 [Energy production and conversion];
43-80 1.58e-05

Cytochrome c5 [Energy production and conversion];


Pssm-ID: 442476 [Multi-domain]  Cd Length: 108  Bit Score: 40.82  E-value: 1.58e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488881347  43 SPAAFSSVDSKKLNANQRKGQQVYSKWCIACHGEGMPG 80
Cdd:COG3245   16 APVGAVALAAAAAAAAARSGEAVYNATCAACHATGVAG 53
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-104 7.54e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 34.21  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488881347   1 MKKIALFF---VLFVCLLNL------NAKDKEwlpkgESISVYEYIPNnprspAAFSSVDSKKLNANQRKGQQVY----S 67
Cdd:PRK03147   1 MKKNRLLFrtiILLILLAAVgytiysNFFADK-----EKVQVGKEAPN-----FVLTDLEGKKIELKDLKGKGVFlnfwG 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488881347  68 KWCIACHGEgMPGTNALSALYKDQG--IPALLEDRTDLS 104
Cdd:PRK03147  71 TWCKPCEKE-MPYMNELYPKYKEKGveIIAVNVDETELA 108
 
Name Accession Description Interval E-value
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
57-82 5.66e-06

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 40.85  E-value: 5.66e-06
                          10        20
                  ....*....|....*....|....*.
gi 488881347   57 ANQRKGQQVYSKWCIACHGEGMPGTN 82
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAGPS 26
CytC5 COG3245
Cytochrome c5 [Energy production and conversion];
43-80 1.58e-05

Cytochrome c5 [Energy production and conversion];


Pssm-ID: 442476 [Multi-domain]  Cd Length: 108  Bit Score: 40.82  E-value: 1.58e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488881347  43 SPAAFSSVDSKKLNANQRKGQQVYSKWCIACHGEGMPG 80
Cdd:COG3245   16 APVGAVALAAAAAAAAARSGEAVYNATCAACHATGVAG 53
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
44-80 6.17e-03

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 34.54  E-value: 6.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488881347  44 PAAFSSVDSKKLNANQRKGQQVYSKWCIACHG---EGMPG 80
Cdd:COG2010   74 LAAAAADAPAADAEALARGKALYEQNCAACHGadgKGGLG 113
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-104 7.54e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 34.21  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488881347   1 MKKIALFF---VLFVCLLNL------NAKDKEwlpkgESISVYEYIPNnprspAAFSSVDSKKLNANQRKGQQVY----S 67
Cdd:PRK03147   1 MKKNRLLFrtiILLILLAAVgytiysNFFADK-----EKVQVGKEAPN-----FVLTDLEGKKIELKDLKGKGVFlnfwG 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488881347  68 KWCIACHGEgMPGTNALSALYKDQG--IPALLEDRTDLS 104
Cdd:PRK03147  71 TWCKPCEKE-MPYMNELYPKYKEKGveIIAVNVDETELA 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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